2JUO
GABPa OST domain
2JUO の概要
| エントリーDOI | 10.2210/pdb2juo/pdb |
| NMR情報 | BMRB: 15451 |
| 分子名称 | GA-binding protein alpha chain (1 entity in total) |
| 機能のキーワード | ost, ubiquitin, transcription factor, nmr ensemble, ga-binding protein, dna-binding, nucleus, transcription regulation, transcription |
| 由来する生物種 | Mus musculus (house mouse) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 9975.39 |
| 構造登録者 | Kang, H.,Nelson, M.L.,Mackereth, C.D.,Schaerpf, M.,Graves, B.J.,McIntosh, L.P. (登録日: 2007-08-31, 公開日: 2008-04-08, 最終更新日: 2024-05-08) |
| 主引用文献 | Kang, H.S.,Nelson, M.L.,Mackereth, C.D.,Scharpf, M.,Graves, B.J.,McIntosh, L.P. Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha J.Mol.Biol., 377:636-646, 2008 Cited by PubMed Abstract: Using NMR spectroscopy, we identified and characterized a previously unrecognized structured domain near the N-terminus (residues 35-121) of the ETS family transcription factor GABP alpha. The monomeric domain folds as a five-stranded beta-sheet crossed by a distorted helix. Although globally resembling ubiquitin, the GABP alpha fragment differs in its secondary structure topology and thus appears to represent a new protein fold that we term the OST (On-SighT) domain. The surface of the GABP alpha OST domain contains two predominant clusters of negatively-charged residues suggestive of electrostatically driven interactions with positively-charged partner proteins. Following a best-candidate approach to identify such a partner, we demonstrated through NMR-monitored titrations and glutathione S-transferase pulldown assays that the OST domain binds to the CH1 and CH3 domains of the co-activator histone acetyltransferase CBP/p300. This provides a direct structural link between GABP and a central component of the transcriptional machinery. PubMed: 18295234DOI: 10.1016/j.jmb.2008.01.054 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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